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Originally published In Press as doi:10.1074/jbc.M301646200 on March 6, 2003

J. Biol. Chem., Vol. 278, Issue 20, 17625-17635, May 16, 2003
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Direct Interaction of Ca2+/Calmodulin Inhibits Histone Deacetylase 5 Repressor Core Binding to Myocyte Enhancer Factor 2*

Imre BergerDagger §, Christoph BieniossekDagger , Christiane Schaffitzel, Markus Hassler, Eugenio Santelli||, and Timothy J. Richmond**

From ETH Zürich, Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, CH-8093 Zürich, Switzerland

Myocyte enhancer factor 2 (MEF2) proteins play a pivotal role in the differentiation of cardiac and skeletal muscle cells. MEF2 factors are regulated by histone deacetylase enzymes such as histone deacetylase 5 (HDAC5). HDAC5 in turn is responsive to Ca2+ signaling mediated by the intracellular calcium sensor calmodulin. Here a combination of proteolytic fragmentation, matrix-assisted laser desorption ionization mass spectrometry, Edman degradation, circular dichroism, gel filtration, and surface plasmon resonance studies is utilized to define and characterize a stable core domain of HDAC5 and to examine its interactions with MEF2a and calmodulin. Results from real time binding experiments provide evidence for direct interaction of Ca2+/calmodulin with HDAC5 inhibiting MEF2a association with this enzyme.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Both authors contributed equally to this work.

§ Recipient of a Liebig fellowship from the Fonds der Chemischen Industrie (Germany).

Supported by the Roche Research Foundation (Switzerland).

|| Present address: The Burnham Institute, 10901 North Torrey Pines Rd., La Jolla, CA 92037.

** To whom correspondence should be addressed. Tel.: 41 1 633 2470; Fax: 41 1 633 1150; E-mail: richmond@mol.biol.ethz.ch.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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